{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Helou L"],"funding":["Ligue Contre le Cancer","Conseil Régional du Centre-Val de Loire","Division of Cancer Prevention, National Cancer Institute","NCI NIH HHS","Société Nationale Française de Gastro-Entérologie"],"pagination":["166805"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC8426422"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["433(7)"],"pubmed_abstract":["PiggyBac(PB)-like elements (pble) are members of a eukaryotic DNA transposon family. This family is of interest to evolutionary genomics because pble transposases have been domesticated at least 9 times in vertebrates. The amino acid sequence of pble transposases can be split into three regions: an acidic N-terminal domain (~100 aa), a central domain (~400 aa) containing a DD[D/E] catalytic triad, and a cysteine-rich domain (CRD; ~90 aa). Two recent reports suggested that a functional CRD is required for pble transposase activity. Here we found that two CRD-deficient pble transposases, a PB variant and an isoform encoded by the domesticated PB-derived vertebrate transposase gene 5 (pgbd5) trigger transposition of the Ifp2 pble. When overexpressed in HeLa cells, these CRD-deficient transpos"],"journal":["Journal of molecular biology"],"pubmed_title":["The C-terminal Domain of piggyBac Transposase Is Not Required for DNA Transposition."],"pmcid":["PMC8426422"],"funding_grant_id":["P30 CA008748","R01 CA214812"],"pubmed_authors":["Helou L","Dardente H","Guillou F","Beauclair L","Buisine N","Kentsis A","Jaszczyszyn Y","Arensburger P","Bigot Y","Lecomte T"],"additional_accession":[]},"is_claimable":false,"name":"The C-terminal Domain of piggyBac Transposase Is Not Required for DNA Transposition.","description":"PiggyBac(PB)-like elements (pble) are members of a eukaryotic DNA transposon family. This family is of interest to evolutionary genomics because pble transposases have been domesticated at least 9 times in vertebrates. The amino acid sequence of pble transposases can be split into three regions: an acidic N-terminal domain (~100 aa), a central domain (~400 aa) containing a DD[D/E] catalytic triad, and a cysteine-rich domain (CRD; ~90 aa). Two recent reports suggested that a functional CRD is required for pble transposase activity. Here we found that two CRD-deficient pble transposases, a PB variant and an isoform encoded by the domesticated PB-derived vertebrate transposase gene 5 (pgbd5) trigger transposition of the Ifp2 pble. When overexpressed in HeLa cells, these CRD-deficient transpos","dates":{"release":"2021-01-01T00:00:00Z","publication":"2021 Apr","modification":"2026-05-09T03:10:58.138Z","creation":"2025-02-18T23:36:40.797Z"},"accession":"S-EPMC8426422","cross_references":{"pubmed":["33450253"],"doi":["10.1016/j.jmb.2020.166805"]}}